Evidence map›Paper›PMID 19783655›Full record

ArticleThe Journal of biological chemistry2009

Palmitoylation of hepatitis C virus core protein is important for virion production.

Nathalie Majeau, Rémi Fromentin, Christian Savard, Marie Duval, Michel J Tremblay, Denis Leclerc

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed, 58 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Nathalie MajeauInfectious Disease Research Centre, CHUL, Université Laval, 2705 boulevard Laurier, Québec G1V 4G2, Canada.
Rémi Fromentin
Christian Savard
Marie Duval
Michel J Tremblay
Denis Leclerc
Centre hospitalier de l'Université Laval · CAUniversité Laval · CAWilfrid Laurier University · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Hepatitis C virus core protein is the viral nucleocapsid of hepatitis C virus. Interaction of core with cellular membranes like endoplasmic reticulum (ER) and lipid droplets (LD) appears to be involved in viral assembly. However, how these interactions with different cellular membranes are regulated is not well understood. In this study, we investigated how palmitoylation, a post-translational protein modification, can modulate the targeting of core to cellular membranes. We show that core is palmitoylated at cysteine 172, which is adjacent to the transmembrane domain at the C-terminal end of core. Site-specific mutagenesis of residue Cys(172) showed that palmitoylation is not involved in the maturation process carried out by the signal peptide peptidase or in the targeting of core to LD. However, palmitoylation was shown to be important for core association with smooth ER membranes and ER closely surrounding LDs. Finally, we demonstrate that mutation of residue Cys(172) in the J6/JFH1 virus genome clearly impairs virion production.

Indexed as

Cell LineCell MembraneCysteineEndoplasmic ReticulumGenome, ViralGenotypeHepacivirusHumansMicroscopy, FluorescenceMutagenesis, Site-DirectedMutationPalmitic AcidProtein Sorting SignalsViral Core ProteinsVirionCysteinenucleocapsid protein, Hepatitis C virusPalmitic AcidProtein Sorting SignalsViral Core Proteins

Identifiers

PMID19783655
PMCPMC2797162
OpenAlexW2041174883

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.